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Rational inhibitor design for Pseudomonas aeruginosa salicylate adenylation enzyme PchD
dc.contributor.author | Shelton, Catherine L. | |
dc.contributor.author | Meneely, Kathleen M. | |
dc.contributor.author | Ronnebaum, Trey A. | |
dc.contributor.author | Chilton, Annemarie S. | |
dc.contributor.author | Riley, Andrew P. | |
dc.contributor.author | Prisinzano, Thomas E. | |
dc.contributor.author | Lamb, Audrey L. | |
dc.date.accessioned | 2023-02-28T15:30:02Z | |
dc.date.available | 2023-02-28T15:30:02Z | |
dc.date.issued | 2022-05-05 | |
dc.identifier.citation | Shelton, C.L., Meneely, K.M., Ronnebaum, T.A. et al. Rational inhibitor design for Pseudomonas aeruginosa salicylate adenylation enzyme PchD. J Biol Inorg Chem 27, 541–551 (2022). https://doi.org/10.1007/s00775-022-01941-8 | en_US |
dc.identifier.uri | http://hdl.handle.net/1808/33962 | |
dc.description.abstract | Pseudomonas aeruginosa is an increasingly antibiotic-resistant pathogen that causes severe lung infections, burn wound infections, and diabetic foot infections. P. aeruginosa produces the siderophore pyochelin through the use of a non-ribosomal peptide synthetase (NRPS) biosynthetic pathway. Targeting members of siderophore NRPS proteins is one avenue currently under investigation for the development of new antibiotics against antibiotic-resistant organisms. Here, the crystal structure of the pyochelin adenylation domain PchD is reported. The structure was solved to 2.11 Å when co-crystallized with the adenylation inhibitor 5′-O-(N-salicylsulfamoyl)adenosine (salicyl-AMS) and to 1.69 Å with a modified version of salicyl-AMS designed to target an active site cysteine (4-cyano-salicyl-AMS). In the structures, PchD adopts the adenylation conformation, similar to that reported for AB3403 from Acinetobacter baumannii. | en_US |
dc.publisher | Springer | en_US |
dc.rights | © The Author(s) 2022. This article is licensed under a Creative Commons Attribution 4.0 International License. | en_US |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | en_US |
dc.subject | Adenylation domain | en_US |
dc.subject | Pseudomonas aeruginosa | en_US |
dc.subject | Inhibitor design | en_US |
dc.subject | Antibiotic resistance | en_US |
dc.subject | Pyochelin | en_US |
dc.title | Rational inhibitor design for Pseudomonas aeruginosa salicylate adenylation enzyme PchD | en_US |
dc.type | Article | en_US |
kusw.kuauthor | Shelton, Catherine L. | |
kusw.kuauthor | Meneely, Kathleen M. | |
kusw.kuauthor | Ronnebaum, Trey A. | |
kusw.kuauthor | Chilton, Annemarie S. | |
kusw.kuauthor | Riley, Andrew P. | |
kusw.kuauthor | Prisinzano, Thomas E. | |
kusw.kuauthor | Lamb, Audrey L. | |
kusw.kudepartment | Molecular Biosciences | en_US |
kusw.kudepartment | Medicinal Chemistry | en_US |
dc.identifier.doi | 10.1007/s00775-022-01941-8 | en_US |
dc.identifier.orcid | https://orcid.org/0000-0002-2352-2130 | en_US |
kusw.oaversion | Scholarly/refereed, publisher version | en_US |
kusw.oapolicy | This item meets KU Open Access policy criteria. | en_US |
dc.identifier.pmid | PMC9470617 | en_US |
dc.rights.accessrights | openAccess | en_US |